6yjr

X-ray diffraction
2.2Å resolution

Crystal structure of unliganded MGAT5 (alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V) luminal domain.

Released:

Function and Biology Details

Reaction catalysed:
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-(beta-D-GlcNAc-(1->4))-alpha-D-Man-(1->3)-(beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6))-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein] = UDP + beta-D-GlcNAc-(1->2)-(beta-D-GlcNAc-(1->4))-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-(beta-D-GlcNAc-(1->6))-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-170784 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A Chains: AAA, BBB
Molecule details ›
Chains: AAA, BBB
Length: 528 amino acids
Theoretical weight: 60.54 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q09328 (Residues: 214-741; Coverage: 71%)
Gene names: GGNT5, MGAT5
Sequence domains: Glycosyltransferase family 18

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 59.809Å b: 100.415Å c: 207.981Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.262
Expression system: Trichoplusia ni